tag for purification
of proteins from E. coli extracts1 because of its high
affinity for immobilized calmodulin (Kd=10-9). CBP fusion
proteins are bound to and eluted from calmodulin affinity matrices at neutral pH
using gentle buffer conditions. A relatively low concentration of Ca2+
ions is required for binding (0.2 to 2.0 mM CaCl2), and proteins are
efficiently eluted upon removal of the calcium with 2 mM EGTA. The CBP tag is
small, (4 kDa) and therefore less likely than some of the larger tags
[e.g., the 26-kDa glutathione-S-transferase (GST) and 40-kDa maltose-binding
protein (MBP) tags] to affect the biological function of the protein of
interest. CBP is efficiently translated in E. coli, and CBP fusion
proteins are typically expressed to high levels. In addition, the CBP tag is
efficiently phosphorylated by protein kinase A and thus, purified CBP fusion
proteins can be readily labeled with isotope and used to probe protein-protein
interactions.2

Despite the advantages of using affinity tags for protein purification, there
are many proteins for which fusion of nonnatural amino acids at the N- or
C-termini adversely affect protein function.3 Most fusion vectors
include short recognition sequences for site-specific proteases that allow
removal of the fusion tag following purification. Many vectors employ target
sequences for proteases that cleave internal to the recognition site and thus,
leave at least one extraneous amino acid fused to the protein of interest. The
use of the protease enterokinase (EK) has the advantage that it cleaves at the
C-terminus of its recognition site, thus when positioned upstream of the protein
of interest, N-terminal purification tags can be completely removed without
leaving any extraneous amino acid residues on the protein of interest. However,
most vectors that employ the use of EK for removal o'"/>

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